How important is the phosphatase activity of sensor kinases?

Research output: Contribution to journalReview article

40 Citations (Scopus)

Abstract

In two-component signaling systems, phosphorylated response regulators (RRs) are often dephosphorylated by their partner kinases in order to control the in vivo concentration of phospho-RR (RR∼P). This activity is easily demonstrated in vitro, but these experiments have typically used very high concentrations of the histidine kinase (HK) compared to the RR∼P. Many two-component systems exhibit exquisite control over the ratio of HK to RR in vivo. The question thus arises as to whether the phosphatase activity of HKs is significant in vivo. This topic will be explored in the present review.

Original languageEnglish (US)
Pages (from-to)168-176
Number of pages9
JournalCurrent Opinion in Microbiology
Volume13
Issue number2
DOIs
StatePublished - Apr 1 2010
Externally publishedYes

Fingerprint

Phosphoric Monoester Hydrolases
Phosphotransferases
Histidine Kinase
In Vitro Techniques

ASJC Scopus subject areas

  • Infectious Diseases
  • Microbiology (medical)
  • Microbiology

Cite this

How important is the phosphatase activity of sensor kinases? / Kenney, Linda.

In: Current Opinion in Microbiology, Vol. 13, No. 2, 01.04.2010, p. 168-176.

Research output: Contribution to journalReview article

@article{b1367fddfe4a40beb07d9e85f0ddee90,
title = "How important is the phosphatase activity of sensor kinases?",
abstract = "In two-component signaling systems, phosphorylated response regulators (RRs) are often dephosphorylated by their partner kinases in order to control the in vivo concentration of phospho-RR (RR∼P). This activity is easily demonstrated in vitro, but these experiments have typically used very high concentrations of the histidine kinase (HK) compared to the RR∼P. Many two-component systems exhibit exquisite control over the ratio of HK to RR in vivo. The question thus arises as to whether the phosphatase activity of HKs is significant in vivo. This topic will be explored in the present review.",
author = "Linda Kenney",
year = "2010",
month = "4",
day = "1",
doi = "10.1016/j.mib.2010.01.013",
language = "English (US)",
volume = "13",
pages = "168--176",
journal = "Current Opinion in Microbiology",
issn = "1369-5274",
publisher = "Elsevier Limited",
number = "2",

}

TY - JOUR

T1 - How important is the phosphatase activity of sensor kinases?

AU - Kenney, Linda

PY - 2010/4/1

Y1 - 2010/4/1

N2 - In two-component signaling systems, phosphorylated response regulators (RRs) are often dephosphorylated by their partner kinases in order to control the in vivo concentration of phospho-RR (RR∼P). This activity is easily demonstrated in vitro, but these experiments have typically used very high concentrations of the histidine kinase (HK) compared to the RR∼P. Many two-component systems exhibit exquisite control over the ratio of HK to RR in vivo. The question thus arises as to whether the phosphatase activity of HKs is significant in vivo. This topic will be explored in the present review.

AB - In two-component signaling systems, phosphorylated response regulators (RRs) are often dephosphorylated by their partner kinases in order to control the in vivo concentration of phospho-RR (RR∼P). This activity is easily demonstrated in vitro, but these experiments have typically used very high concentrations of the histidine kinase (HK) compared to the RR∼P. Many two-component systems exhibit exquisite control over the ratio of HK to RR in vivo. The question thus arises as to whether the phosphatase activity of HKs is significant in vivo. This topic will be explored in the present review.

UR - http://www.scopus.com/inward/record.url?scp=77949916191&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77949916191&partnerID=8YFLogxK

U2 - 10.1016/j.mib.2010.01.013

DO - 10.1016/j.mib.2010.01.013

M3 - Review article

VL - 13

SP - 168

EP - 176

JO - Current Opinion in Microbiology

JF - Current Opinion in Microbiology

SN - 1369-5274

IS - 2

ER -